11Beta-hydroxysteroid dehydrogenase activity in progesterone biotransformation by the filamentous fungus Cochliobolus lunatus.
Progesterone biotransformation was examined in relation to hydroxylating and dehydrogenating enzymes of Cochliobolus lunatus. 11beta-hydroxysteroid dehydrogenase activity (11beta-HSD) was located in cytosolic fraction and was NADP-dependent, inducible by progesterone and apparently uni-directional. Several inhibitors of 11beta-hydroxysteroid dehydrogenase were tested; furosemide, glycyrrhizic-acid and carbenoxolone did not influence the dehydrogenation of 11beta-hydroxy-4-pregnene-3,20-dione to 4-pregnene-3,11,20-trione, although grapefruit juice significantly reduced the rate of progesterone hydroxylation.
Vitas
M
M
Medical Centre for Molecular Biology, Institute of Biochemistry, Medical Faculty, Ljubljana, Slovenia.
Pajic
T
T
Kelly
S L
SL
Komel
R
R
D042842:11-beta-Hydroxysteroid Dehydrogenases; D001203:Ascomycota / Q000201:enzymology*; D001628:Beverages; D001711:Biotransformation; D002957:Citrus; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D006913:Hydroxysteroid Dehydrogenases / Q000378:metabolism*; D011374:Progesterone / Q000493:pharmacokinetics*
D011374:Progesterone; D003577:Cytochrome P-450 Enzyme System; D006913:Hydroxysteroid Dehydrogenases; D042842:11-beta-Hydroxysteroid Dehydrogenases